Draw a hydropathy plot and a 2D protein cartoon for a protein that passes through the lipid bilayer 6 times
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Draw a hydropathy plot and a 2D protein cartoon for a protein that passes through the lipid bilayer 6 times..
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- The given protein, Protein X, is a heterotrimer - meaning it is a multimeric protein consisting of different polypeptide chains. Its molecular weight is 200 kDa. Using SDS-PAGE, the protein was characterized and the following profile is the result (attached in the picture). 1: Standard Protein Ladder 2: Protein X solution 3: Protein X solution + β-mercaptoethanol Determine the molecular weights of the three subunits of protein X based on the gel profile. Write the MW of each subunit and explain the obtained answer.Describe the following levels of protein organization and give an example of each: A.) Primary B.) Secondary C.) Tertiary D.) QuarternaryOn an SDS-gel, If the distance traveled by the bromophenol blue dye is 7 cm, and the distance traveled by the protein band is 2.1 cm, the mobility of the protein is 0.3 30 3 30%
- Based on the characteristic given, determine which level of protein structure is being referred to. 3D arrangement of localized regions of proteins A. PRIMARY B. SECONDARYDescribe the 4 levels of protein structure: primary, secondary, tertiary and quaternary. And, note which will be disrupted by application of heat.Give an example of a protein containing primarily betapleated sheets. Is this a fibrous or globular protein?
- Explain why the torned lipid bilayer is not sealed itself by forming a hemi-micelle cap at the edges.Describe in detail the vapour diffusion method for crystallising a proteinYou analyze a protein of 100 kDa using SDS-PAGE in the absence and presence of �-mercaptoethanol (BME) and observe the following band pattern in the gels: Which of the following statements about the protein is correct? (the image is attached) a. The protein consists of three polypeptide chains, two of which are connected via S-S bridges. b. The protein consists of two different polypeptide chains connected via S-S bridges. c. The protein has two different folding conformations. d. The protein consists of two different polypeptide chains linked to each other via non-covalent interactions.
- The given protein, Protein X, is a heterotrimer - meaning it is a multimeric protein consisting of different polypeptide chains. Its molecular weight is 200 kDa. Using SDS-PAGE, the protein was characterized and the following profile is the result (attached in the picture). 1: Standard Protein Ladder 2: Protein X solution 3: Protein X solution + β-mercaptoethanol Based on the given gel profile in the picture, can it be concluded that the solution of Protein X is pure? Explain. can it be concluded that disulfide bonds hold together Protein X's quaternary structure? Explain.In the following diagram of a portion of a protein, label the types of interactions that are shown. What level of protein structure are these interactions producing? ____________________Partition or thin layer chromatography separates proteins on the basis of polarity with polar amino acids being retained on the stationary phase. Rank the following in order, with least mobile amino acid first. Cys Ile His Asn